Analytical Data
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Gene name
Outer membrane 蛋白 A/OmpA
- Application
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Alternative Names
ompA; omp1B; Major outer membrane porin; serovar B; MOMP
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Species
Chlamydia trachomatis
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23421
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Expression Region
23-394aa
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Molecular Weight
47.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
OmpA (Outer Membrane Protein A) is a well-studied protein found in the outer membrane of various Gram-negative bacteria, including Escherichia coli. It plays a crucial role in maintaining the structural integrity of the bacterial membrane and is involved in important physiological processes such as nutrient transport and adhesion to surfaces. The study of OmpA has gained significant attention due to its potential applications in vaccine development, as it can elicit strong immune responses. Recombinant OmpA protein has been generated through molecular cloning and expression techniques, allowing researchers to obtain large quantities of this protein for further analysis. The investigation of OmpA also contributes to our understanding of bacterial pathogenesis, as its expression levels can influence virulence factor production and biofilm formation. Moreover, OmpA serves as a model for studying protein folding and membrane insertion, providing insights into the broader mechanisms of outer membrane assembly in bacteria. The ongoing research on OmpA recombinant protein explores its structural properties, immunogenicity, and potential as a target for novel antibacterial therapies, making it a significant focus in microbiology and immunology.
